Temperature dependent michaelis-menten analysis of the bovine adenosine deaminase­ catalyzed deamination of adenosine

Title:Temperature dependent michaelis-menten analysis of the bovine adenosine deaminase­ catalyzed deamination of adenosine

Volume: 7 Issue: 3

Author(s): Christian Castro and B. Mark Britt*

Affiliation:

• Department of Chemistry and Biochemistry, P.O.Box 97348, Baylor University, Waco, TX 76798 USA

Abstract: Michaelis-Menten analysis of the bovine adenosine deaminase catalyzed deamination of adenosine from 10.0 - 40.0°C and at its pH optimum (pH=6.3) is reported. It is found that increases gradually and nearly linearly with T and exhibits a minimum between 10 and 15°C. The relative increase ofk... with Tis more pronounced and very linear. Values at the physiologic T of 38.3°C are: KM= 26±2 µM; k..,, = 99±4 s·1• The pseudosecond order rate constant (k../K has a maximal value of-3.8 µM·1s·1 in the physiological temperature range.

Cite this article as:

Castro Christian and Britt Mark B.*, Temperature dependent michaelis-menten analysis of the bovine adenosine deaminase­ catalyzed deamination of adenosine, Protein & Peptide Letters 2000; 7 (3) . https://dx.doi.org/10.2174/092986650703221206123057